ID   EXG_PICAN               Reviewed;         435 AA.
AC   Q12626;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Glucan 1,3-beta-glucosidase;
DE            EC=3.2.1.58;
DE   AltName: Full=Exo-1,3-beta-glucanase;
DE   Flags: Precursor;
OS   Pichia angusta (Yeast) (Hansenula polymorpha).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Pichiaceae; Ogataea.
OX   NCBI_TaxID=870730;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 14754 / CBS 1976 / JCM 3620 / NBRC 0799 / NCYC 495 / NRRL
RC   Y-1798 / VKM Y-1397;
RX   PubMed=10029988;
RX   DOI=10.1002/(sici)1097-0061(19990130)15:2<91::aid-yea343>3.0.co;2-#;
RA   Esteban P.F., Vazquez de Aldana C.R., del Rey F.;
RT   "Cloning and characterization of 1,3-beta-glucanase-encoding genes from
RT   non-conventional yeasts.";
RL   Yeast 15:91-109(1999).
CC   -!- FUNCTION: Beta-glucanases participate in the metabolism of beta-glucan,
CC       the main structural component of the cell wall. It could also function
CC       biosynthetically as a transglycosylase (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Successive hydrolysis of beta-D-glucose units from the non-
CC         reducing ends of (1->3)-beta-D-glucans, releasing alpha-glucose.;
CC         EC=3.2.1.58;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC       {ECO:0000305}.
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DR   EMBL; Z46868; CAA86948.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q12626; -.
DR   SMR; Q12626; -.
DR   CAZy; GH5; Glycoside Hydrolase Family 5.
DR   CLAE; EXG5A_PICAN; -.
DR   PhylomeDB; Q12626; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004338; F:glucan exo-1,3-beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   InterPro; IPR001547; Glyco_hydro_5.
DR   InterPro; IPR018087; Glyco_hydro_5_CS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF00150; Cellulase; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
PE   3: Inferred from homology;
KW   Cell wall biogenesis/degradation; Disulfide bond; Glycosidase; Hydrolase;
KW   Secreted; Signal; Zymogen.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..435
FT                   /note="Glucan 1,3-beta-glucosidase"
FT                   /id="PRO_0000007886"
FT   ACT_SITE        222
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        323
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   DISULFID        306..432
FT                   /evidence="ECO:0000250"
FT   DISULFID        331..357
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   435 AA;  49264 MW;  840C22F271CC87A0 CRC64;
     MLFPVLHLPK AMKFSSFSLI ASSLLSLVAA APVTLLKRDS RWDYANDKIY GVNIGGWLVL
     EPFITPSLFE AVSSDVPVDE YHYTEALGKE EAEKRLQEHW STWIKEEDFK GMANAGLNFV
     RIPIGYWAFQ LAEGDPYVQG QQEYLDKALE WCAKYGLKAW VDLHGAPGSQ NGFDNSGKRG
     EIGWQNTTGY VDLTVQVLDQ LTSKYGGSNY SDVIIGIELL NEPLGSYLDF DQLVDFYNKG
     YQLVRNNGNA PVIIHDAYLP DHTFDNVLNT EQDPNVWEVI VDHHHYQVFD EGSLSQSIDE
     HVSTACGWGQ SENTEYHYSL CGEWTAALTD CAKWLNGAGR GARYDATFGG GNYIGSCDQL
     YTANYDYFTP EVISNYRRYV EAQMDSFLYG KNAGWVFWCW KTENTIEWDM QRLLGLGIIP
     QPLDDRQYPN QCGFS